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Search results

1000 results found for “Transferrin”

Name

Description

Product #

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  • View Data Sheet

    Name :

    CTHRC1 Human

    Description:

    Collagen Triple Helix Repeat Containing 1 Human Recombinant

    Collagen Triple Helix Repeat Containing 1, Protein NMTC1, CTHRC1.

    Product # :

    PRO-2027

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    Description

    CTHRC1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 234 amino acids (31-243 a.a) and having a molecular mass of 25.3kDa.CTHRC1 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    CTHRC1 protein solution (1mg/ml) containing 20mM Tris-HCl (pH 8.0) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Collagen triple helix repeat-containing protein 1 (CTHRC1) functions as a negative regulator of collagen matrix deposition. CTHRC1 is a secreted 28kDa protein which is glycosylated and highly conserved from lower chordates to mammals. CTHRC1 is highly connected with calcified tissues and cartilaginous matrix, but not with endothelial cells. CTHRC1 is detected qualitatively in plasma of healthy human subjects. CTHRC1 plasma levels are also significantly elevated during pregnancy, in diabetes, in inflammatory and infectious conditions, in subjects with acute myeloid leukemia but not in subjects with solid cancers. The hormonal functions of CTHRC1 include regulation of lipid storage and cellular glycogen levels with potentially far-reaching implications for cell metabolism and physiology. CTHRC1 gene deletion leads to fatty liver (steatosis) formation in mice while others exhibited inactivation of the CTHRC1 gene also results in low bone mass.

    • Synonyms

      Collagen Triple Helix Repeat Containing 1, Protein NMTC1, CTHRC1.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MSEIPKGKQK AQLRQREVVD LYNGMCLQGP AGVPGRDGSP GANGIPGTPG IPGRDGFKGE KGECLRESFE ESWTPNYKQC SWSSLNYGID LGKIAECTFT KMRSNSALRV LFSGSLRLKC RNACCQRWYF TFNGAECSGP LPIEAIIYLD QGSPEMNSTI NIHRTSSVEG LCEGIGAGLV DVAIWVGTCS DYPKGDASTG WNSVSRIIIE ELPK.

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Cthrc1 Human
  • View Data Sheet

    Name :

    MRRF Human

    Description:

    Mitochondrial Ribosome Recycling Factor Human Recombinant

    MRFF, MTRRF, RRF, Ribosome-recycling factor, mitochondrial, Ribosome-releasing factor, mitochondrial.

    Product # :

    PRO-1299

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    Description

    MRRF Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 228 amino acids (56-262 a.a.) and having a molecular mass of 25.1kDa.MRRF is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    MRRF protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer, (pH 8.0), 0.2M NaCl, 30% glycerol and 2mM DTT.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Mitochondrial Ribosome Recycling Factor (MRRF) is a member of the RRF family. MRRF attaches to the large ribosomal subunit in the cleft which has a peptidyl transferase center. MRRF controls the release of ribosome from messenger RNA at the termination of protein biosynthesis. Also, it may intensify the efficacy of translation by recycling ribosome from one round of translation to another.

    • Synonyms

      MRFF, MTRRF, RRF, Ribosome-recycling factor, mitochondrial, Ribosome-releasing factor, mitochondrial.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MATKKAKAKG KGQSQTRVNI NAALVEDIIN LEEVNEEMKS VIEALKDNFN KTLNIRTSPG SLDKIAVVTA DGKLALNQIS QISMKSPQLI LVNMASFPEC TAAAIKAIRE SGMNLNPEVE GTLIRVPIPQ VTREHREMLV KLAKQNTNKA KDSLRKVRTN SMNKLKKSKD TVSEDTIRLI EKQISQMADD TVAELDRHLA VKTKELLG.

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Mrrf Human
  • View Data Sheet

    Name :

    SULT2A1 Human

    Description:

    Sulfotransferase Family, Cytosolic, 2A, Member 1 Human Recombinant

    Sulfotransferase family cytosolic 2A dehydroepiandrosterone (DHEA)-preferring member 1, DHEA-ST, STD, HST, ST2, ST2A1, ST2A3, Alcohol/hydroxysteroid sulfotransferase, bile-salt sulfotranasferase 2A1, EC 2.8.2.14.

    Product # :

    ENZ-141

    Price :

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    Description

    SULT2A1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 305 amino acids (1-285a.a) and having a molecular mass of 35.9kDa.SULT2A1 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    SULT2A1 protein solution (1mg/1ml) containing 20mM Tris-HCl buffer (pH8.0), 20% glycerol, 0.1M NaCl and 1mM DTT.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      SULT2A1 is a member fo the sulfotransferase family. SULT2A1 is primarily expressed in liver and adrenal tissues, and to a lesser extent in kidney. SULT2A1 catalyzes the 3'-phosphoadenosine 5'-phosphosulfate-dependent sulfation of an extensive selection of steroids in human liver and adrenal tissues, and in addition is responsible for a larg number of the sulfation of bile acids in human liver.

    • Synonyms

      Sulfotransferase family cytosolic 2A dehydroepiandrosterone (DHEA)-preferring member 1, DHEA-ST, STD, HST, ST2, ST2A1, ST2A3, Alcohol/hydroxysteroid sulfotransferase, bile-salt sulfotranasferase 2A1, EC 2.8.2.14.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MSDDFLWFEG IAFPTMGFRS ETLRKVRDEF VIRDEDVIIL TYPKSGTNWL AEILCLMHSK GDAKWIQSVP IWERSPWVES EIGYTALSET ESPRLFSSHL PIQLFPKSFF SSKAKVIYLM RNPRDVLVSG YFFWKNMKFI KKPKSWEEYF EWFCQGTVLY GSWFDHIHGW MPMREEKNFL LLSYEELKQD TGRTIEKICQ FLGKTLEPEE LNLILKNSSF QSMKENKMSN YSLLSVDYVV DKAQLLRKGV SGDWKNHFTV AQAEDFDKLF QEKMADLPRE LFPWE

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Sult2A1 Human
  • View Data Sheet

    Name :

    TAF15 Human

    Description:

    TAF15 Human Recombinant

    Npl3, RBP56, TAF2N, TAFII68, TATA-binding protein-associated factor 2N, 68 kDa TATA-binding protein-associated factor, RNA-binding protein 56, TAF15.

    Product # :

    PRO-1805

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    Description

    TAF15 Human Recombinant produced in E. coli is. a single polypeptide chain containing 282 amino acids (148-406) and having a molecular mass of 30kDa. TAF15 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The TAF15 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 30% glycerol and 1mM DTT.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      TAF15 is a member of the TET family of RNA-binding proteins. TAF15 is a component of a subset of multi-subunit transcription initiation factor TFIID complexes which takes part in RNA polymerase II gene transcription. Translocations involving TAF15 are found in severe leukemia and extraskeletal myxoid chondrosarcoma. Mutations in TAF15 take part in amyotrophic lateral sclerosis.

    • Synonyms

      Npl3, RBP56, TAF2N, TAFII68, TATA-binding protein-associated factor 2N, 68 kDa TATA-binding protein-associated factor, RNA-binding protein 56, TAF15.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSSYHSQRE NYSHHTQDDR RDVSRYGEDN RGYGGSQGGG RGRGGYDKDG RGPMTGSSGG DRGGFKNFGG HRDYGPRTDA DSESDNSDNN TIFVQGLGEG VSTDQVGEFF KQIGIIKTNK KTGKPMINLY TDKDTGKPKG EATVSFDDPP SAKAAIDWFD GKEFHGNIIK VSFATRRPEF MRGGGSGGGR RGRGGYRGRG GFQGRGGDPK SGDWVCPNPS CGNMNFARRN SCNQCNEPRP EDSRPSGGDF RGRGYGGERG YR.

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Taf15 Human
  • View Data Sheet

    Name :

    FUR E.Coli

    Description:

    Ferric Uptake Regulator E.Coli Recombinant

    ECs0714, Ferric uptake regulation protein, Ferric uptake regulator, Z0831, FUR, ECK0671, JW0669, b0683.

    Product # :

    PRO-622

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    • description
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    Description

    Ferric Uptake Regulator Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 148 amino acids and having a molecular mass of 16.7kDa.

    Source

    Escherichia Coli.

    Formulation

    The Ferric Uptake Regulator protein solution (1mg/ml) contains 20mM Tris-HCl pH-8, 2mM CaCl2 and 100mM NaCl.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Ferric Uptake Regulator protein NCBI Accession No.: NP_415209 is a DNA-binding protein which controls iron-responsive genes. Ferric Uptake Regulator has a molecular mass of 17-kDa and plays a role in global transcriptional repressor that in the existence of iron regulates functions as diverse as iron acquisition, oxidative stress, and virulence. In Escherichia coli, members of the Ferric Uptake Regulator family regulate the expression of at least 100 genes that function in processes as diverse as the biosynthesis and transport of siderophores, the expression of virulence factors, the alleviation of oxidative and NO-induced stress, and the inhibition of ferritin production through the expression of RyhB.

    • Synonyms

      ECs0714, Ferric uptake regulation protein, Ferric uptake regulator, Z0831, FUR, ECK0671, JW0669, b0683.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MTDNNTALKK AGLKVTLPRL KILEVLQEPD NHHVSAEDLY KRLIDMGEEI GLATVYRVLN QFDDAGIVTR HNFEGGKSVF ELTQQHHHDH LICLDCGKVI EFSDDSIEAR QREIAAKHGI RLTNHSLYLY GHCAEGDCRE DEHAHEGK.

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    Ferric Uptake Regulator
  • View Data Sheet

    Name :

    PNMT Human

    Description:

    Phenylethanolamine-N-Methyltransferase Human Recombinant

    PENT, PNMTase, Noradrenaline-N-methyltransferase, Phenylethanolamine N-methyltransferase, PNMT, MGC34570.

    Product # :

    ENZ-457

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    Description

    Recombinant Human PNMT produced in E.Coli is a single, non-glycosylated polypeptide chain containing 282 amino acids (1-282 a.a.) and having a molecular mass of 30.8 kDa.PNMT is purified by conventional chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The PNMT protein solution contains 20mM Tris-HCl, pH-8 & 10% Glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      PNMT is an enzyme located in the adrenal medulla and it catalyzes the final step of the catecholamine biosynthesis pathway. PNMT has beta-carboline 2N-methyltransferase activity. PNMT takes part in regulating epinephrine production. Glucocorticoid receptors form multimers of PNMT independent of the DNA binding domain. PNMT expression is regulated late in mouse gestation by AP2-alpha and glucocorticoids.

    • Synonyms

      PENT, PNMTase, Noradrenaline-N-methyltransferase, Phenylethanolamine N-methyltransferase, PNMT, MGC34570.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MSGADRSPNA GAAPDSAPGQ AAVASAYQRF EPRAYLRNNY APPRGDLCNP NGVGPWKLRC LAQTFATGEV SGRTLIDIGS GPTVYQLLSA CSHFEDITMT DFLEVNRQEL GRWLQEEPGA FNWSMYSQHA CLIEGKGECW QDKERQLRAR VKRVLPIDVH QPQPLGAGSP APLPADALVS AFCLEAVSPD LASFQRALDH ITTLLRPGGH LLLIGALEES WYLAGEARLT VVPVSEEEVR EALVRSGYKV RDLRTYIMPA HLQTGVDDVK GVFFAWAQKV GL.

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    Pnmt Human
  • View Data Sheet

    Name :

    TOMM34 Human

    Description:

    Translocase Of Outer Mitochondrial Membrane 34 Human Recombinant

    HTOM34P, TOM34, URCC3, Mitochondrial import, TOMM34 receptor subunit TOM34, hTom34, Translocase of outer membrane 34 kDa subunit.

    Product # :

    PRO-1501

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    Description

    TOMM34 Human Recombinant produced in E. coli is a single polypeptide chain containing 332 amino acids (1-309) and having a molecular mass of 36.9kDa. TOMM34 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The TOMM34 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 20% glycerol and 1mM DTT.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      Translocase of Outer Mitochondrial Membrane 34 (TOMM34) which is found in the cytoplasm and sometimes associated with the outer mitochondrial membrane is involved in the import of precursor proteins into mitochondria. TOMM34 has a chaperone-like activity, binding the mature portion of unfolded proteins and aiding their import into mitochondria. TOMM34 has a weak ATPase activity and contains 6 TPR repeats.

    • Synonyms

      HTOM34P, TOM34, URCC3, Mitochondrial import, TOMM34 receptor subunit TOM34, hTom34, Translocase of outer membrane 34 kDa subunit.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSMAPKFPD SVEELRAAGN ESFRNGQYAE ASALYGRALR VLQAQGSSDP EEESVLYSNR AACHLKDGNC RDCIKDCTSA LALVPFSIKP LLRRASAYEA LEKYPMAYVD YKTVLQIDDN VTSAVEGINR MTRALMDSLG PEWRLKLPSI PLVPVSAQKR WNSLPSENHK EMAKSKSKET TATKNRVPSA GDVEKARVLK EEGNELVKKG NHKKAIEKYS ESLLCSNLES ATYSNRALCY LVLKQYTEAV KDCTEALKLD GKNVKAFYRR AQAHKALKDY KSSFADISNL LQIEPRNGPA QKLRQEVKQN LH.

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    Tomm34 Human
  • View Data Sheet

    Name :

    GMNN Human

    Description:

    Geminin Human Recombinant

    GMNN, Geminin, DNA Replication Inhibitor, Gem, RP3-369A17.3.

    Product # :

    PRO-579

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    Description

    Geminin Human Recombinant fused to N-terminal His-Tag produced in E.Coli is a single, non-glycosylated polypeptide chain containing 245 amino acids and having a molecular mass of 27.7 kDa.

    Source

    Escherichia Coli.

    Formulation

    The protein solution contains 20mM Tris pH 8, 100mM NaCl and 10% glycerol.

    Purity

    Greater than 95.0% as determined by:
    (a) Analysis by RP-HPLC.
    (b) Analysis by SDS-PAGE.

    More Info

    • Introduction

      Geminin is a 25 kDa nuclear protein, which inhibits DNA replication and is degraded during the mitotic phase of the cell cycle. Geminin controls replication by binding to the licensing factor Cdt1, and is involved in neural differentiation. In addition, Geminin directly interacts with Six3 and Hox homeodomain proteins during embryogenesis and inhibits their functions. Geminin can also promote DNA replication. Geminin has 2 roles in 2 different stages of the cell cycle: Geminin is a negative regulator of DNA replication during the “S phase” of the cell cycle. Inhibition of Geminin during the “S phase” (by RNAi) results in an additional round of replication of portions of the genome. During the “M phase” of the cell cycle (mitosis) Geminin stabilizes the replication factor Cdt1 promoting DNA replication during the next cell cycle. Moreover, inhibition of Geminin during mitosis (by RNAi) causes destabilization of Cdt1 protein and impairment of DNA replication during the next cell cycle. Geminin thus guarantees that only one round of replication occurs during each cell cycle. It was discovered that Geminin is overexpressed in a number of malignancies and cancer cell lines. This maintains the concept that Geminin has also a positive role in DNA replication and cell cycle progression. Geminin accumulates through S, G2 and M phases of the cell cycle but is absent during the G1 phase. During the metaphase/anaphase transition of mitosis Geminin levels decrease.

    • Synonyms

      GMNN, Geminin, DNA Replication Inhibitor, Gem, RP3-369A17.3.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSMNPS MKQKQEEIKE NIKNSSVPRR TLKMIQPSAS GSLVGRENEL SAGLSKRKHR NDHLTSTTSS PGVIVPESSE NKNLGGVTQE SFDLMIKENP SSQYWKEVAE KRRKALYEAL KENEKLHKEI EQKDNEIARL KKENKELAEV AEHVQYMAEL IERLNGEPLD NFESLDNQEF DSEEETVEDS LVEDSEIGTC AEGTVSSSTD
      AKPCI.

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    Geminin Human
  • View Data Sheet

    Name :

    GST, His

    Description:

    Glutathione S-Transferase Recombinant, His Tag

    Glutathione S-Transferase, GST, Glutathione S-transferase class-mu 28 kDa isozyme, GST 28, EC 2.5.1.18, Sj28GST, Sj28 antigen.

    Product # :

    ENZ-451

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    Description

    Recombinant Schistosoma japonicum GST full length protein contains a total of 244 amino acids (1-218 a.a.) expressed in E.coli, having a molecular mass of 28.3kDa. The GST protein is fused to a 20 amino acids His-Tag at N-terminus. The GST protein is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    GST is supplied in PBS pH 7.4 & 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Biological Activity

    >10 units/mg, & is defined as the amount of enzyme that conjugate 1.0 u mole of 1-chloro-2,4-dinitrobenzene (CDNB) with reduced glutathione per minute at pH-6.5 at 25C.

    More Info

    • Introduction

      Antioxidant enzyme Glutathione S- Transferase (GST) is thought to do the primary cellular defense mechanism against reactive oxygen species. GST reduces lipid hydroperoxides through its Se-independent glutathione peroxidase activity. The enzyme also detoxifies lipid peroxidation end products such as 4-hydroxynonenal (4-HNE).
      The soluble GST is a 26 kDa protein which occurs as a dimer in all aerobic organisms. Each monomer has two domains, one that binds GSH and is an /-structure similar to thioredoxin and the other, all helical, that binds the hydrophobic substrate. The GST -fusion protein expression system is a widely used recombinant protein expression system that allows a peptide or a regulatory protein domain to be expressed as a fusion to the C-terminus of Schistosoma japonicum GST. Fusion proteins also possess GST -enzymatic activity and can undergo dimerization similar to in vivo. The fusion protein can be purified via GST -affinity column chromatography. In most cases, the desired peptides or domains are removed from GST by applying a specific protease that recognizes and cleaves the linker between the protein domain and GST. The technique has been widely used to generate different kinds of proteins for crystallization, molecular immunology studies, the production of vaccines and studies involving protein-protein and protein-DNA interactions.

    • Synonyms

      Glutathione S-Transferase, GST, Glutathione S-transferase class-mu 28 kDa isozyme, GST 28, EC 2.5.1.18, Sj28GST, Sj28 antigen.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MSPILGYWKI KGLVQPTRLL LEYLEEKYEE HLYERDEGDK WRNKKFELGL EFPNLPYYID GDVKLTQSMAIIRYIADKHN MLGGCPKERA EISMLEGAVL DIRYGVSRIA YSKDFETLKV DFLSKLPEML KMFEDRLCHK TYLNGDHVTH PDFMLYDALDVVLYMDPMCL DAFPKLVCFK KRIEAIPQID KYLKSSKYIA WPLQGWQATF GGGDHPPKSD LVPR.

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    Glutathione S Transferase His
  • View Data Sheet

    Name :

    GSTK1 Human

    Description:

    Glutathione S-Transferase Kappa 1 Human Recombinant

    GST13, GST13-13, GSTK1-1, GST class-kappa, EC 2.5.1.18, Glutathione S-transferase kappa 1, Glutathione S-transferase subunit 13, hGSTK1, GSTK1.

    Product # :

    ENZ-476

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    Description

    GSTK1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 226 amino acids (1-226 a.a.) and having a molecular mass of 25.5 kDa. GSTK1 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    GSTK1 solution containing 20mM Tris pH-8, 1mM DTT and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      GSTK1 is involved in cellular detoxification. GSTK1 is localized to the peroxisome and catalyzes the conjugation of the thiol group of glutathione (GSH) to the electrophilic groups of a broad range of hydrophobic substrates, leading to an easier removal of the latter from the cells.

    • Synonyms

      GST13, GST13-13, GSTK1-1, GST class-kappa, EC 2.5.1.18, Glutathione S-transferase kappa 1, Glutathione S-transferase subunit 13, hGSTK1, GSTK1.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MGPLPRTVEL FYDVLSPYSW LGFEILCRYQ NIWNINLQLR PSLITGIMKD SGNKPPGLLP RKGLYMANDL KLLRHHLQIP IHFPKDFLSV MLEKGSLSAM RFLTAVNLEH PEMLEKASRE LWMRVWSRNE DITEPQSILA AAEKAGMSAE QAQGLLEKIA TPKVKNQLKE TTEAACRYGA FGLPITVAHV DGQTHMLFGS DRMELLAHLL GEKWMGPIPP AVNARL.

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    Gstk1 Human
  • View Data Sheet

    Name :

    EPO, Clone PAT1C12AT

    Description:

    Erythropoietin clone PAT1C12AT, Mouse Anti Human

    EPO-a, EPO-alpha, Epoetin, EP, MGC138142.

    Product # :

    ANT-744

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    Formulation

    1mg/ml containing PBS, pH-7.4, 10% Glycerol and 0.02% Sodium Azide.

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    • Introduction

      EPO is a member of the EPO/TPO family and encodes a secreted, glycosylated cytokine composed of 4 alpha helical bundles. EPO is found in the plasma and regulates red cell production by promoting erythroid differentiation and initiating hemoglobin synthesis. EPO also has neuroprotective activity against a variety of potential brain injuries and antiapoptotic functions in several tissue types.

    • Synonyms

      EPO-a, EPO-alpha, Epoetin, EP, MGC138142.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

      For periods up to 1 month store at 4°C, for longer periods of time, store at -20°C. Prevent freeze thaw cycles

    • Ig Subclass

      Mouse IgG1 heavy chain and k light chain.

    • Clone

      PAT1C12AT.

    • Type

      Mouse Anti Human Monoclonal.

    • Purification Method

      EPO antibody was purified from mouse ascitic fluids by protein-A affinity chromatography.

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    Epo Antibody
  • View Data Sheet

    Name :

    TGFB1 (113 a.a.) Human

    Description:

    Transforming Growth Factor-Beta 1 (113 a.a.) Human Recombinant

    Transforming growth factor beta-1, TGF-beta-1, CED, DPD1, TGFB, TGF-b 1.

    Product # :

    CYT-679

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    Description

    TGF-b 1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 113 amino acids (279-390 a.a.) and having a total molecular mass of 12.9 kDa. TGF-b 1 (113 a.a.) is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The TGF-b 1 solution contains 10mM Sodium Citrate (pH3.5) and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Transforming growth factor betas (TGFBetas) mediate many cell-cell interactions that occur during embryonic development. Three TGFBetas have been identified in mammals. TGFBeta1, TGFBeta2 and TGFBeta3 are each synthesized as precursor proteins that are very similar in that each is cleaved to yield a 112 amino acid polypeptide that remains associated with the latent portion of the molecule.

    • Synonyms

      Transforming growth factor beta-1, TGF-beta-1, CED, DPD1, TGFB, TGF-b 1.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MALDTNYCFS STEKNCCVRQ LYIDFRKDLG WKWIHEPKGY HANFCLGPCP YIWSLDTQYS KVLALYNQHN PGASAAPCCV PQALEPLPIVYYVGRKPKVE QLSNMIVRSC KCS.

    • Background

      Title: Transforming Growth Factor-Beta 1 (113 a.a.) Human Recombinant: A Key Regulator of Cellular Processes with Therapeutic Potential

      Abstract:


      Transforming Growth Factor-Beta 1 (TGF-β1) is a multifunctional cytokine that plays a crucial role in various cellular processes, including cell growth, differentiation, and immune modulation. The development of TGF-β1 human recombinant proteins has provided valuable tools for studying its biological functions and therapeutic applications. This research paper explores the production process, characteristics, and potential therapeutic uses of TGF-β1 human recombinant, highlighting its importance and clinical significance.

      Introduction:


      TGF-β1 is a pivotal cytokine involved in numerous physiological and pathological processes, such as embryonic development, tissue repair, and immune regulation. Harnessing the therapeutic potential of TGF-β1 has been facilitated by the development of TGF-β1 human recombinant proteins using recombinant DNA technology. These recombinant proteins have become valuable tools for investigating the biological functions of TGF-β1 and exploring its therapeutic applications.

      Production Process and Characteristics:


      TGF-β1 human recombinant proteins are produced using recombinant DNA technology, allowing for the expression of the TGF-β1 gene in different host systems. The resulting recombinant proteins possess similar structural and functional characteristics to native TGF-β1. They exhibit the ability to bind to the TGF-β receptor, initiate intracellular signaling pathways, and modulate various cellular responses.

      Therapeutic Applications:


      TGF-β1 human recombinant proteins have shown promise in a wide range of therapeutic applications. They have been investigated for their potential in tissue regeneration and wound healing, as TGF-β1 plays a crucial role in promoting cell proliferation and extracellular matrix production. Additionally, TGF-β1 has been studied in the context of fibrotic diseases, such as pulmonary fibrosis and liver fibrosis, where it is implicated in the fibrotic cascade. Furthermore, TGF-β1 has been explored as a potential target for antitumor therapies due to its involvement in tumor progression and immune evasion.

      Advantages and Challenges:


      The use of TGF-β1 human recombinant proteins offers several advantages, including the ability to study and manipulate its biological functions in a controlled manner. Recombinant proteins also provide a consistent and reproducible source of TGF-β1, overcoming the challenges associated with sourcing native TGF-β1 from biological samples. However, challenges remain in optimizing production processes, ensuring correct protein folding, and maintaining protein stability.

      Conclusion:


      TGF-β1 human recombinant proteins have emerged as valuable tools for studying the biological functions of TGF-β1 and exploring its therapeutic applications. The production of TGF-β1 recombinant proteins using recombinant DNA technology allows for the investigation of its diverse roles in cellular processes. The therapeutic potential of TGF-β1 human recombinant proteins extends to tissue regeneration, fibrotic diseases, and cancer research. Continued research and development efforts are essential to further optimize production processes, address challenges, and fully exploit the clinical benefits of TGF-β1 human recombinant proteins.

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    Tgf Beta 1 Human 113 Aa
  • View Data Sheet

    Name :

    ANXA1 Human

    Description:

    Annexin A1 Human Recombinant

    ANX1, LPC1, ANXA1, Lipocortin I, Calpactin II, Chrombindin-9, p35, Annexin-1, Phospholipase A2 inhibitory protein, Annexin I, Annexin A1.

    Product # :

    PRO-679

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    Description

    ANXA1 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 346 amino acids (1-346 a.a.) and having a molecular mass of 38.7 kDa.ANXA1 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The ANXA1 protein solution contains 20mM Tris-HCl, pH-8, 100mM NaCl, 1mM DTT and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      ANXA1 is part of the family of Ca(2+)-dependent phospholipid binding proteins which have a Mw between 35kDa-40kDa and are situated on the cytosolic face of the plasma membrane. ANXA1 protein has a Mw of 40kDa, with phospholipase A2 inhibitory activity to bind from two to four calcium ions with high affinity. Since phospholipase A2 is necessary for the biosynthesis of the potent mediators of inflammation, prostaglandins and leukotrienes, ANXA1 might have potential anti-inflammatory activity. ANXA1 promotes membrane fusion and iplays a role in exocytosis. The recognition of ANXA1 protein by immunocytochemical leads a simple, highly sensitive and specific assay for diagnosis of hairy cell leukemia.

    • Synonyms

      ANX1, LPC1, ANXA1, Lipocortin I, Calpactin II, Chrombindin-9, p35, Annexin-1, Phospholipase A2 inhibitory protein, Annexin I, Annexin A1.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MAMVSEFLKQ AWFIENEEQE YVQTVKSSKG GPGSAVSPYP TFNPSSDVAA LHKAIMVKGV DEATIIDILT KRNNAQRQQI KAAYLQETGK
      PLDETLKKAL TGHLEEVVLA LLKTPAQFDA DELRAAMKGL GTDEDTLIEI LASRTNKEIR DINRVYREEL KRDLAKDITS DTSGDFRNAL
      LSLAKGDRSE DFGVNEDLAD SDARALYEAG ERRKGTDVNV FNTILTTRSY PQLRRVFQKY TKYSKHDMNK VLDLELKGDI EKCLTAIVKCATSKPAFFAE KLHQAMKGVG TRHKALIRIM VSRSEIDMND IKAFYQKMYG ISLCQAILDE TKGDYEKILV ALCGGN.

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    Anxa1 Human
  • View Data Sheet

    Name :

    SERPINC1 Human, Sf9

    Description:

    Serpin Peptidase Inhibitor, Clade C Member 1 Human Recombinant, Sf9

    SERPINC1, AT3, AT3D, ATIII, THPH7, Antithrombin-III, Serpin C1.

    Product # :

    PRO-2541

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    Description

    SERPINC Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 441 amino acids (33-464a.a.) and having a molecular mass of 50.1kDa (Molecular size on SDS-PAGE will appear at approximately 50-70kDa). SERPINC is expressed with a 9 amino acids His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    SERPINC protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Serpin Peptidase Inhibitor, Clade C Member 1 (SERPINC1), which is a part of the serpin superfamily, is a plasma protease inhibitor. SERPINC1 inhibits thrombin and other activated serine proteases of the coagulation system, and regulates the blood coagulation cascade. SERPINC1 also inhibits Thrombin and Factors IXa, Xa and XIa. Deficiencies in SERPINC1 can cause ATIII deficiency, an autosomal dominant disease which might lead to a hereditary thrombophilia.

    • Synonyms

      SERPINC1, AT3, AT3D, ATIII, THPH7, Antithrombin-III, Serpin C1.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      ADPHGSPVDI CTAKPRDIPM NPMCIYRSPE KKATEDEGSE QKIPEATNRR VWELSKANSR FATTFYQHLA DSKNDNDNIF LSPLSISTAF AMTKLGACND TLQQLMEVFK FDTISEKTSD QIHFFFAKLN CRLYRKANKS SKLVSANRLF GDKSLTFNET YQDISELVYG AKLQPLDFKE NAEQSRAAIN KWVSNKTEGR ITDVIPSEAI NELTVLVLVN TIYFKGLWKS KFSPENTRKE LFYKADGESC SASMMYQEGK FRYRRVAEGT QVLELPFKGD DITMVLILPK PEKSLAKVEK ELTPEVLQEW LDELEEMMLV VHMPRFRIED GFSLKEQLQD MGLVDLFSPE KSKLPGIVAE GRDDLYVSDA FHKAFLEVNE EGSEAAASTA VVIAGRSLNP NRVTFKANRP FLVFIREVPL NTIIFMGRVA NPCVKHHHHH H.

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Serpinc1 Protein 2
  • View Data Sheet

    Name :

    EFNA5 Human, Active

    Description:

    Ephrin A5 Human Recombinant, Active

    EFNA5, AF1, EFL5, EPLG7, GLC1M, LERK7, RAGS, Ephrin-A5, AL-1, EPH-related receptor tyrosine kinase ligand 7.

    Product # :

    PRO-2816

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    Description

    EFNA5 Human Recombinant is a single, glycosylated, polypeptide chain (21-203 a.a) containing a total of 422 amino acids and having a molecular mass of 48.1 kDa. EFNA5 is fused to a 239 a.a hIgG-His-Tag at C-terminus and is purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    The EFNA5 solution (0.5mg/ml) contains 10% Glycerol and Phosphate-Buffered Saline (pH 7.4).

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    The ED50 range ≤ 60 ng/ml measured by its binding ability in a functional ELISA with Mouse EphA3 (CAT# pro-2817).

    More Info

    • Synonyms

      EFNA5, AF1, EFL5, EPLG7, GLC1M, LERK7, RAGS, Ephrin-A5, AL-1, EPH-related receptor tyrosine kinase ligand 7.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      QDPGSKAVAD RYAVYWNSSN PRFQRGDYHI DVCINDYLDV FCPHYEDSVP EDKTERYVLY MVNFDGYSAC DHTSKGFKRW ECNRPHSPNG PLKFSEKFQL FTPFSLGFEF RPGREYFYIS SAIPDNGRRS CLKLKVFVRP TNSCMKTIGV HDRVFDVNDK VENSLEPADD TVHESAEPSR GENLEPKSCD KTHTCPPCPA PELLGGPSVF LFPPKPKDTL MISRTPEVTC VVVDVSHEDP EVKFNWYVDG VEVHNAKTKP REEQYNSTYR VVSVLTVLHQ DWLNGKEYKC KVSNKALPAP IEKTISKAKG QPREPQVYTL PPSRDELTKN QVSLTCLVKG FYPSDIAVEW ESNGQPENNY KTTPPVLDSD GSFFLYSKLT VDKSRWQQGN VFSCSVMHEA LHNHYTQKSL SLSPGKHHHH HH.

    • Background

      EFNA5 functions through contact-mediated signaling, which can result in either forward signaling (through Eph receptors) or reverse signaling (through ephrins themselves). These signaling pathways regulate various cellular processes such as migration, adhesion, and proliferation. Disruptions or alterations in EFNA5 signaling have been implicated in neurodevelopmental disorders, cancer metastasis, and angiogenesis, highlighting the importance of understanding this protein's roles at a molecular level.

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Efna5 Protein
  • View Data Sheet

    Name :

    EREG Human, HEK

    Description:

    Epiregulin Human Recombinant, HEK

    EPR, Epiregulin, Ep, ER, Proepiregulin, EREG.

    Product # :

    CYT-1206

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    Description

    EREG Human Recombinant produced in HEK293 cells is a single, glycosylated polypeptide chain (63-108a.a) containing 289 amino acids and having a molecular mass of 32.6 kDa.EREG is fused to a 239 amino acid hIgG-His-Tag at C-terminus & purified by proprietary chromatographic techniques.

    Source

    HEK293 cells.

    Formulation

    EREG protein (0.25mg/ml) contains 10% glycerol and Phosphate-Buffered Saline (pH 7.4).

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    Measured in a cell proliferation assay using Balb/3T3 mouse embryonic fibroblast cells. The ED50 range ≤ 1ug/ml.

    More Info

    • Introduction

      "Epiregulin is part of the EGF family. Epiregulin functions as a ligand of EGFR, as well as a ligand of most members of the ERBB (v-erb-b2 oncogene homolog) family of tyrosine-kinase receptors.Epiregulin is expressed mostly in the placenta and peripheral blood leukocytes and in specific carcinomas of the bladder, lung, kidney and colon. Epiregulin stimulates the proliferation of keratinocytes, hepatocytes, fibroblasts and vascular smooth muscle cells. Epiregulin inhibits the growth of several tumor-derived epithelial cell lines. Human Epiregulin is initially synthesized as a glycosylated 19.0 kDa transmembrane precursor protein, which is processed by proteolytic cleavage to produce a 6.0 kDa mature secreted sequence."

    • Synonyms

      EPR, Epiregulin, Ep, ER, Proepiregulin, EREG.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks.Store, frozen at -20°C for longer periods of time.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      DGSMVSITKC SSDMNGYCLH GQCIYLVDMS QNYCRCEVGY TGVRCEHFFL LEPKSCDKTH TCPPCPAPEL LGGPSVFLFP PKPKDTLMIS RTPEVTCVVV DVSHEDPEVK FNWYVDGVEV HNAKTKPREE QYNSTYRVVS VLTVLHQDWL NGKEYKCKVS NKALPAPIEK TISKAKGQPR EPQVYTLPPS RDELTKNQVS LTCLVKGFYP SDIAVEWESN GQPENNYKTT PPVLDSDGSF FLYSKLTVDK SRWQQGNVFS CSVMHEALHN HYTQKSLSLS PGKHHHHHH

    • Background

      What is the molecular weight/Mw of EREG Protein?
      EREG Protein has a total Mw of 32.6kDa.

      What is the source or expression system of EREG Protein?
      HEK293 cells.

      What is the Purity of EREG Protein?
      EREG Protein is >90% pure as determined by SDS-PAGE.

      What is the Biological Activity of EREG Protein?
      Measured in a cell proliferation assay using Balb/3T3 mouse embryonic fibroblast cells. The ED50 range ≤ 1ug/ml.

      What is the amino acid sequence of EREG Protein?
      DGSMVSITKC SSDMNGYCLH GQCIYLVDMS QNYCRCEVGY TGVRCEHFFL LEPKSCDKTH TCPPCPAPEL LGGPSVFLFP PKPKDTLMIS RTPEVTCVVV DVSHEDPEVK FNWYVDGVEV HNAKTKPREE QYNSTYRVVS VLTVLHQDWL NGKEYKCKVS NKALPAPIEK TISKAKGQPR EPQVYTLPPS RDELTKNQVS LTCLVKGFYP SDIAVEWESN GQPENNYKTT PPVLDSDGSF FLYSKLTVDK SRWQQGNVFS CSVMHEALHN HYTQKSLSLS PGKHHHHHH

      What applications can EREG Protein be used in?
      EREG Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for EREG Protein?
      The endotoxin level is minimal, EREG Protein was purified using conventional chromatography techniques.

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Ereg Human
  • View Data Sheet

    Name :

    MTHFS Human

    Description:

    5,10-Methenyltetrahydrofolate Synthetase Human Recombinant

    5,10-methenyltetrahydrofolate synthetase (5-formyltetrahydrofolate cyclo-ligase), HsT19268, Methenyl-THF synthetase, FLJ30410, EC 6.3.3.2.

    Product # :

    ENZ-096

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    Description

    MTHFS produced in E.Coli is a single, non-glycosylated polypeptide chain containing 223 amino acids (1-203a.a.) and having a molecular mass of 25.4 kDa. MTHFS is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The MTHFS protein solution (0.5mg/1ml) is formulated in 20mM Tris-HCl buffer (pH8.0), 200mM NaCl, 5mM DTT and 30% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      MTHFS is a cytosolic protein which takes part in the formate metabolic process. MTHFS along with a magnesium cofactor catalyzes the ATP-dependent reaction which reduces 5-formyltetrahydrofolate (5-MTHF) to 5,10-methenyltetrahydrofolate(MTHF). MTHF is the substrate used by MTHFR (methylenetetrahydrofolate reductase) to generate 5-MTHF. In addition, MTHF is a coenzyme used in thymidine biosynthesis by thymidylate synthase (FAD).

    • Synonyms

      5,10-methenyltetrahydrofolate synthetase (5-formyltetrahydrofolate cyclo-ligase), HsT19268, Methenyl-THF synthetase, FLJ30410, EC 6.3.3.2.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MAAAAVSSAK RSLRGELKQR LRAMSAEERL RQSRVLSQKV IAHSEYQKSK RISIFLSMQD EIETEEIIKD IFQRGKICFI PRYRFQSNHM DMVRIESPEE ISLLPKTSWN IPQPGEGDVR EEALSTGGLD LIFMPGLGFD KHGNRLGRGK GYYDAYLKRC LQHQEVKPYT LALAFKEQIC LQVPVNENDM KVDEVLYEDS STA

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Mthfs Human
  • View Data Sheet

    Name :

    Treponema TP0453

    Description:

    Outer Membrane Protein Treponema pallidum Recombinant

    Outer membrane protein TP0453, 30kLP, TP_0453, TPANIC_0453

    Product # :

    TRP-255

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    Description

    Recombinant Treponema pallidum Outer Membrane Protein TP0453 has a Mw of 26kDa, and was purified from E. coli.The Recombinant Treponema pallidum Outer Membrane Protein TP0453 is fused to 6 amino acid His tag at its C terminal and purified by proprietary chromatographic technique.

    Source

    Escherichia Coli.

    Formulation

    Treponema TP0453 solution contains 25mM K2CO3 with PBS.

    Purity

    Protein is >95% pure as determined by SDS-PAGE (coomassie staining).

    More Info

    • Introduction

      Tp0453 is a carrier of lipids and glycolipids during outer membrane. Tp045 is hypothesized to be a new type of bacterial outer membrane protein, which reduces T.pallidum outer membrane permeability to nutrients while remaining inaccessible to antibodies. Tp0453 exhibited 100% specificity and sensitivity in reaction with syphilis patients’ sera, giving negative result with Lyme disease, relapsing-fever or leptospirosis patients’ sera.

    • Synonyms

      Outer membrane protein TP0453, 30kLP, TP_0453, TPANIC_0453

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks.Store, frozen at -20°C for longer periods of time.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Applications

      Rapid test, Immunoassay.

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Tp0453 Treponema
  • View Data Sheet

    Name :

    Recombinant TNF-a Antibody

    Description:

    Recombinant Anti Human Tumor Necrosis Factor-Alpha

    Product # :

    ANT-599

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    Description

    Recombinant TNF-a Antibody is a recombinant human IgG1 monoclonal antibody specific for human tumor necrosis factor (TNF). Recombinant TNF-a Antibody is produced by recombinant DNA technology in a Chinese Hamster Ovary mammalian cell expression system in a serum-free medium and has a molecular weight of approximately 148 kDa.

    Source

    CHO.

    Formulation

    The Recombinant TNF-a Antibody 53mg/ml solution contains 6.16 mg/ml of sodium chloride, 0.86 mg/ml of monobasic sodium phosphate dihydrate, 1.53 mg/ml of dibasic sodium phosphate dihydrate, 0.3 mg/ml of sodium citrate, 1.30 mg/ml of citric acidmonohydrate, 12 mg/ml of mannitol, 1mg/ml of polysorbate 80, pH-5.

    Purity

    Greater than 98.0% as determined by:
    (a) Analysis by SEC-HPLC.
    (b) Analysis by SDS-PAGE.

    Biological Activity

    The EC50 as determined by L929 cell proliferation assay for neutralization reaction between TNF-a Antibody and TNFA, Perform a comparison of a dilution series of the Sample solution with a dilution series of the Standard solution, measured potency was found to be 1.2 X 104EU/mg.

    More Info

    • Introduction

      Tumor necrosis factor is a cytokine involved in systemic inflammation and is a member of a group of cytokines that all stimulate the acute phase reaction. TNF is mainly secreted by macrophages.
      TNF causes apoptotic cell death, cellular proliferation, differentiation, inflammation, tumorigenesisand viral replication, TNF is also involved in lipid metabolism, and coagulation. TNF's primary role is in the regulation of immune cells.
      Dysregulation and, in particular, overproduction of TNF have been implicated in a variety of human diseases- autoimmune diseases, insulin resistance, and cancer.

    • Physical Appearance

      Clear and colorless solution.

    • Stability

      Recombinant TNF-a Antibody should be stored between 2-8°C and should be protected from light. DO NOT FREEZE. DO NOT SHAKE.

    • Amino Acid Sequence

      LIGHT CHAIN
      DIQMTQSPSSLSASVGDRVTITCRASQGIRNYLAWYQQKPGKAPKLLIYAASTLQSGVPSRFSGSGSGTDF
      TLTISSLQPEDVATYYCQRYNRAPYTFGQGTKVEIKRTVAAPSVFIFPPSDEQLKSGTASVVCLLNNFYPR
      EAKVQWKVDNALQSGNSQESVTEQDSKDSTYSLSSTLTLSKADYEKHKVYACEVTHQGLSSPVTKSFNRGEC

      HEAVY CHAIN
      EVQLVESGGGLVQPGRSLRLSCAASGFTFDDYAMHWVRQAPGKGLEWVSAITWNSGHIDYADSVEGRFTISR
      DNAKNSLYLQMNSLRAEDTAVYYCAKVSYLSTASSLDYWGQGTLVTVSSASTKGPSVFPLAPSSKSTSGGTA
      ALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVD
      KKVEPKSCDKTHTCPPCPAPELLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVKFNWYVDGVEV
      HNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPSRD
      ELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVM
      HEALHNHYTQKSLSLSPGK.

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Recombinant Tnf A Antibody
  • View Data Sheet

    Name :

    Exendin 4

    Description:

    Exendin-4 Recombinant

    Product # :

    HOR-269

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    Description

    Exendin-4 Recombinant produced in E.Coli is a non-glycosylated polypeptide chain containing 39 amino acids and having a molecular mass of approximately 4.2kDa. Exendin-4 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2μm filtered concentrated solution in PBS, pH 7.4.

    Purity

    Greater than 96.0% as determined by:
    (a) Analysis by RP-HPLC.
    (b) Analysis by SDS-PAGE.

    Biological Activity

    1. Regulates Glucose levels rapidly
    2. Reduces Insulin resistance 
    3. Reduces Glucagon

    4. Stimulates beta cell growth production.

    More Info

    • Introduction

      Exedin-4 Recombinant is a like peptide-1 receptor agonist. The native hormone is produced in the gut of Gila monster Heloderma suspectrum (a type of reptile found in the desert) that stimulates production without causing threateningly low blood sugar, which can occur after using some anti-diabetes products. Recently, researchers used extracted saliva from gila monsters to create an unprecedented breakthrough in Diabetes Type 2 treatment. Unlike other products taken for type 2 diabetes, Exedin-4 has not been linked with weight gain and actually resulted in weight loss, according to the researchers. Exedin-4 enhances glucose-dependant secretion, suppresses inappropriately elevated secretion and slows gastric emptying in vivo. It also promotes B-cell proliferation and neogenesis in vitro and in animal models. Exedin-4 stimulates an increase in acinar cAMP, without stimulating the release of amylase.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Exendin Recombinant although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Exendin-4 should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized Exendin Recombinant in sterile 18MΩ-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      HGEGTFTSDL SKQMEEEAVR LFIEWLKNGG PSSGAPPPS.

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Exendin 4
  • View Data Sheet

    Name :

    HPRT PAT1D9AT Antibody

    Description:

    Hypoxanthine-Guanine Phosphoribosyltransferase Clone PAT1D9AT, Mouse Anti Human

    Hypoxanthine-Guanine Phosphoribosyltransferase , EC 2.4.2.8, HGPRT, HGPRTase, HPRT, HPRT1.

    Product # :

    ANT-727

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    • More Info

    Formulation

    1mg/ml containing PBS, pH-7.4, 10% Glycerol and 0.02% Sodium Azide.

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    • Introduction

      HPRT1 has a main part in the generation of purine nucleotides through the purine salvage pathway. HPRT1 primarily functions to salvage purines from degraded DNA to renewed purine synthesis. Therefore, it performs as a catalyst in the reaction between guanine and phosphoribosyl pyrophosphate to form GMP.

    • Synonyms

      Hypoxanthine-Guanine Phosphoribosyltransferase , EC 2.4.2.8, HGPRT, HGPRTase, HPRT, HPRT1.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Immunogen

      Anti-human HPRT mAb, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with recombinant human HPRT amino acids 1-218 purified from E. coli.

    • Ig Subclass

      Mouse IgG2b heavy chain and κ light chain.

    • Clone

      PAT1D9AT.

    • Applications

      HPRT antibody has been tested by ELISA, Western blot analysis, ICC/IF and Flow cytometry to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results.

    • Type

      Mouse Anti Human Monoclonal.

    • Storage Procedures

      For periods up to 1 month store at 4°C, for longer periods of time, store at -20°C. Prevent freeze thaw cycles.

    • Purification Method

      HPRT antibody was purified from mouse ascitic fluids by protein-A affinity chromatography.

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Hprt1 Antibody
  • View Data Sheet

    Name :

    GOT1 Antibody

    Description:

    Glutamic-Oxaloacetic Transaminase 1, Mouse Anti Human

    EC 2.6.1.1, Aspartate aminotransferase 1, Transaminase A, GIG18.

    Product # :

    ANT-496

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    • More Info

    Formulation

    1mg/ml containing PBS, pH-7.4, 10% Glycerol and 0.02% Sodium Azide.

    More Info

    • Introduction

      GOT1 is a pyridoxal phosphate-dependent enzyme which exists in cytoplasmic and mitochondrial forms, GOT1 and GOT2, which participate in amino acid metabolism and the urea and tricarboxylic acid cycles. Both enzymes are homodimeric and show close homology.

    • Synonyms

      EC 2.6.1.1, Aspartate aminotransferase 1, Transaminase A, GIG18.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Immunogen

      Anti-human GOT1 mAb, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with recombinant human GOT1 amino acids 1-413 purified from E. coli.

    • Ig Subclass

      Mouse IgG2a heavy chain and ? light chain.

    • Clone

      PAT3G11AT.

    • Applications

      GOT1 antibody has been tested by ELISA, Western blot analysis, Flow cytometry and ICC/IF to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results.

    • Type

      Mouse Anti Human Monoclonal.

    • Storage Procedures

      For periods up to 1 month store at 4°C, for longer periods of time, store at -20°C. Prevent freeze thaw cycles.

    • Purification Method

      GOT1 antibody was purified from mouse ascitic fluids by protein-A affinity chromatography.

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Got1 Antibody
  • View Data Sheet

    Name :

    TGM2 Human

    Description:

    Tissue Transglutaminase Human Recombinant

    Protein gamma-glutamyltransferase 2, EC 2.3.2.13, Tissue transglutaminase, TGase C, TGC, TG(C), Transglutaminase-2, TGase-H, TG2, TGM2.

    Product # :

    ENZ-394

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    Description

    Tissue Transglutaminase Human Recombinant produced in E.coli is a non-glycosylated, polypeptide chain having a molecular mass of 78,018 Dalton. tTG is expressed with a -6xHis tag and purified by proprietary chromatographic techniques. By point mutation of the active center the catalytic transglutaminase activity has been eliminated, resulting in increased stability during storage and coating.

    Source

    Escherichia Coli.

    Formulation

    TGM2 is supplied in 16mM HEPES buffer pH-8.0, 400mM NaCl, and 20% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      Celiac disease is an enteropathy that is characterized by intestinal lesions of variable severity. Tissue-type transglutaminase (tTG) is believed to be the predominant autoantigen for celiac disease and the corresponding autoantibodies show higher sensitivity and specificity than anti-gliadin antibodies. Highly pure recombinant human tTG is now available to replace the traditionally used tTG fraction from guinea pig.
      Tissue-type transglutaminase antigens have been specifically modified for improved handling: exchange of an active site amino acid eliminates the protein cross-linking activity of the enzyme, while maintaining the native three-dimensional structure and the enzyme's secondary GTPase activity. This engineering assures reproducible properties of the antigen preparations through the absence of variable and ill-defined covalent aggregates of tTG antigen and host cell proteins.

    • Synonyms

      Protein gamma-glutamyltransferase 2, EC 2.3.2.13, Tissue transglutaminase, TGase C, TGC, TG(C), Transglutaminase-2, TGase-H, TG2, TGM2.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. Avoid multiple freeze-thaw cycles.

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Tgm2 Human
  • View Data Sheet

    Name :

    GLYATL2 Human

    Description:

    Glycine-N-Acyltransferase-Like 2 Human Recombinant

    BXMAS2-10, GATF-B, Glycine N-acyltransferase-like protein 2, Acyl-CoA:glycine N-acyltransferase-like protein 2, GLYATL2.

    Product # :

    ENZ-770

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    Description

    GLYATL2 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 317 amino acids (1-294a.a) and having a molecular mass of 36.7kDa. GLYATL2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The GLYATL2 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl, 50% glycerol and 2mM DTT.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      Glycine-N-Acyltransferase-Like 2 (GLYATL2) is a part of the glycine N-acyltransferase family expressed mainly in salivary gland and trachea. GLYATL2 is a mitochondrial acyltransferase that transfers the acyl group to the N-terminus of glycine. GLYATL2 conjugates numerous substrates, like arachidonoyl-CoA and saturated medium and longchain acyl-CoAs ranging from chain-length C8:0-CoA to C18:0-CoA, to form a variety of N-acylglycines. GLYATL2 also shows a preference for monounsaturated fatty acid oleoyl-CoA (C18:1-CoA) as an acyl donor.

    • Synonyms

      BXMAS2-10, GATF-B, Glycine N-acyltransferase-like protein 2, Acyl-CoA:glycine N-acyltransferase-like protein 2, GLYATL2.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSMLVLHNS QKLQILYKSL EKSIPESIKV YGAIFNIKDK NPFNMEVLVD AWPDYQIVIT RPQKQEMKDD QDHYTNTYHI FTKAPDKLEE VLSYSNVISW EQTLQIQGCQ EGLDEAIRKV ATSKSVQVDY MKTILFIPEL PKKHKTSSND KMELFEVDDD NKEGNFSNMF LDASHAGLVN EHWAFGKNER SLKYIERCLQ DFLGFGVLGP EGQLVSWIVM EQSCELRMGY TVPKYRHQGN MLQIGYHLEK YLSQKEIPFY FHVADNNEKS LQALNNLGFK ICPCGWHQWK CTPKKYC.

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Glyatl2 Human
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